pubmed-article:20038579 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:20038579 | lifeskim:mentions | umls-concept:C0085828 | lld:lifeskim |
pubmed-article:20038579 | lifeskim:mentions | umls-concept:C0024337 | lld:lifeskim |
pubmed-article:20038579 | lifeskim:mentions | umls-concept:C0079904 | lld:lifeskim |
pubmed-article:20038579 | lifeskim:mentions | umls-concept:C1456820 | lld:lifeskim |
pubmed-article:20038579 | lifeskim:mentions | umls-concept:C1367731 | lld:lifeskim |
pubmed-article:20038579 | lifeskim:mentions | umls-concept:C1150587 | lld:lifeskim |
pubmed-article:20038579 | lifeskim:mentions | umls-concept:C1705632 | lld:lifeskim |
pubmed-article:20038579 | lifeskim:mentions | umls-concept:C1150571 | lld:lifeskim |
pubmed-article:20038579 | lifeskim:mentions | umls-concept:C1417830 | lld:lifeskim |
pubmed-article:20038579 | lifeskim:mentions | umls-concept:C1514216 | lld:lifeskim |
pubmed-article:20038579 | lifeskim:mentions | umls-concept:C1546857 | lld:lifeskim |
pubmed-article:20038579 | lifeskim:mentions | umls-concept:C1879547 | lld:lifeskim |
pubmed-article:20038579 | lifeskim:mentions | umls-concept:C1556066 | lld:lifeskim |
pubmed-article:20038579 | lifeskim:mentions | umls-concept:C1619636 | lld:lifeskim |
pubmed-article:20038579 | lifeskim:mentions | umls-concept:C1514873 | lld:lifeskim |
pubmed-article:20038579 | pubmed:issue | 8 | lld:pubmed |
pubmed-article:20038579 | pubmed:dateCreated | 2010-2-15 | lld:pubmed |
pubmed-article:20038579 | pubmed:abstractText | Transforming growth factor-beta-activated kinase 1 (TAK1) plays an essential role in the tumor necrosis factor alpha (TNFalpha)- and interleukin-1beta (IL-1beta)-induced IkappaB kinase (IKK)/nuclear factor-kappaB (NF-kappaB) and c-Jun N-terminal kinase (JNK)/activator protein 1 (AP-1) activation. Here we report that TNFalpha and IL-1beta induce Lys(63)-linked TAK1 polyubiquitination at the Lys(158) residue within the kinase domain. Tumor necrosis factor receptor-associated factors 2 and 6 (TRAF2 and -6) act as the ubiquitin E3 ligases to mediate Lys(63)-linked TAK1 polyubiquitination at the Lys(158) residue in vivo and in vitro. Lys(63)-linked TAK1 polyubiquitination at the Lys(158) residue is required for TAK1-mediated IKK complex recruitment. Reconstitution of TAK1-deficient mouse embryo fibroblast cells with TAK1 wild type or a TAK1 mutant containing a K158R mutation revealed the importance of this site in TNFalpha and IL-1beta-mediated IKK/NF-kappaB and JNK/AP-1 activation as well as IL-6 gene expression. Our findings demonstrate that Lys(63)-linked polyubiquitination of TAK1 at Lys(158) is essential for its own kinase activation and its ability to mediate its downstream signal transduction pathways in response to TNFalpha and IL-1beta stimulation. | lld:pubmed |
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pubmed-article:20038579 | pubmed:language | eng | lld:pubmed |
pubmed-article:20038579 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:20038579 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:20038579 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:20038579 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:20038579 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:20038579 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:20038579 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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pubmed-article:20038579 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:20038579 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:20038579 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:20038579 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:20038579 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:20038579 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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pubmed-article:20038579 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:20038579 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:20038579 | pubmed:month | Feb | lld:pubmed |
pubmed-article:20038579 | pubmed:issn | 1083-351X | lld:pubmed |
pubmed-article:20038579 | pubmed:author | pubmed-author:VigPP | lld:pubmed |
pubmed-article:20038579 | pubmed:author | pubmed-author:JinS GSG | lld:pubmed |
pubmed-article:20038579 | pubmed:author | pubmed-author:ToyP HPH | lld:pubmed |
pubmed-article:20038579 | pubmed:author | pubmed-author:ZhangHongH | lld:pubmed |
pubmed-article:20038579 | pubmed:author | pubmed-author:SchneiderMich... | lld:pubmed |
pubmed-article:20038579 | pubmed:author | pubmed-author:YangYuY | lld:pubmed |
pubmed-article:20038579 | pubmed:author | pubmed-author:FuSongbinS | lld:pubmed |
pubmed-article:20038579 | pubmed:author | pubmed-author:ChangAlexA | lld:pubmed |
pubmed-article:20038579 | pubmed:author | pubmed-author:GeNinglingN | lld:pubmed |